Research workbench
AlphaFold monomer V2.0 prediction for D-lactate dehydrogenase (P26297)
Analyse AlphaFold monomer V2.0 prediction for D-lactate dehydrogenase (P26297) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P26297
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x032de8ecd31921A4EaFf7f09A852178F9c639617
- UniProt
- P26297
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 333 | — | P26297 |
Compared structures
- 1J49 · Insights into domain closure, substrate specificity and catalysis of D-lactate… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1J49 · Insights into domain closure, substrate specificity and catalysis of D-lactate… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1J4A · Insights into domain closure, substrate specificity and catalysis of D-lactate… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1J4A · Insights into domain closure, substrate specificity and catalysis of D-lactate… · an experimental structure of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P26297
- Elsewhere: UniProt P26297 · AlphaFold DB P26297
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